Molecular characterization of <i>Saccharomyces cerevisiae</i> Sco2p reveals a high degree of redundancy with Sco1p

Lode, Anja; Paret, Claudia; Rödel, Gerhard

doi:10.1002/yea.883

Cited by 38 publications

(28 citation statements)

References 42 publications

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“…This observation suggests that the residues separating the transmembrane helix from the folded domain are essential to promote dimerization. In vivo studies also have shown that this N-terminal region is crucial for yeast Sco1 function and cannot be replaced, even by its Sco2 counterpart (20).…”

Section: Resultsmentioning

confidence: 99%

A hint for the function of human Sco1 from different structures

Banci

Bertini

Calderone

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

101

162

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The solution structures of apo, Cu(I), and Ni(II) human Sco1 have been determined. The protein passes from an open and conformationally mobile state to a closed and rigid conformation upon metal binding as shown by electrospray ionization MS and NMR data. The metal ligands of Cu(l) are two Cys residues of the CPXXCP motif and a His residue. The latter is suitably located to coordinate the metal anchored by the two Cys residues. The coordination sphere of Ni(II) in solution is completed by another ligand, possibly Asp. Crystals of the Ni(II) derivative were also obtained with the Ni(II) ion bound to the same His residue and to the two oxidized Cys residues of the CPXXCP motif. We propose that the various structures solved here represent the various states of the protein in its functional cycle and that the metal can be bound to the oxidized protein at a certain stage. Although it now seems reasonable that Sco1, which is characterized by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function

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Section: Resultsmentioning

confidence: 99%

A hint for the function of human Sco1 from different structures

Banci

Bertini

Calderone

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

101

162

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“…Similarly, energy-minimized homology models of hSCO2 and the R. spheroides homolog, PrrC, also indicate a predominately negative surface (data not shown). Because Lode et al (30,31) reported a stable complex between yeast Cox2p and Sco1p/Sco2p, we mapped the electrostatic potential of subunit II from bovine COX (32). Interestingly, this surface is also negatively charged (data not shown).…”

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confidence: 96%

Crystal Structure of Human SCO1

Williams¹,

Sue²,

Banting

et al. 2005

Journal of Biological Chemistry

112

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Human SCO1 and SCO2 are copper-binding proteins involved in the assembly of mitochondrial cytochrome c oxidase (COX). We have determined the crystal structure of the conserved, intermembrane space core portion of apo-hSCO1 to 2.8 Å. It is similar to redox active proteins, including thioredoxins (Trx) and peroxiredoxins (Prx), with putative copper-binding ligands located at the same positions as the conserved catalytic residues in Trx and Prx. SCO1 does not have disulfide isomerization or peroxidase activity, but both hSCO1 and a sco1 null in yeast show extreme sensitivity to hydrogen peroxide. Of the six missense mutations in SCO1 and SCO2 associated with fatal mitochondrial disorders, one lies in a highly conserved exposed surface away from the copper-binding region, suggesting that this region is involved in protein-protein interactions. These data suggests that SCO functions not as a COX copper chaperone, but rather as a mitochondrial redox signaling molecule.

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“…More precisely, Sco2 contains "electron transport" and "bipartite nuclear localization signal" motifs in ORF0 and ORF‫,1מ‬ respectively. It is similar to Sco1p and may have a redundant function with Sco1p in delivery of copper to cytochrome c oxidase; it interacts with Cox2p (Lode et al 2002). Surprisingly, yeast two-hybrid assays also show it interacts with Cyclin-B (Ito et al 2001).…”

Section: Discussionmentioning

confidence: 99%

Identification of programmed translational -1 frameshifting sites in the genome of Saccharomyces cerevisiae

Bekaert¹

2005

Genome Res.

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Frameshifting is a recoding event that allows the expression of two polypeptides from the same mRNA molecule. Most recoding events described so far are used by viruses and transposons to express their replicase protein. The very few number of cellular proteins known to be expressed by a −1 ribosomal frameshifting has been identified by chance. The goal of the present work was to set up a systematic strategy, based on complementary bioinformatics, molecular biology, and functional approaches, without a priori knowledge of the mechanism involved. Two independent methods were devised. The first looks for genomic regions in which two ORFs, each carrying a protein pattern, are in a frameshifted arrangement. The second uses Hidden Markov Models and likelihood in a two-step approach. When this strategy was applied to the Saccharomyces cerevisiae genome, 189 candidate regions were found, of which 58 were further functionally investigated. Twenty-eight of them expressed a full-length mRNA covering the two ORFs, and 11 showed a −1 frameshift efficiency varying from 5% to 13% (50-fold higher than background), some of which corresponds to genes with known functions. From other ascomycetes, four frameshifted ORFs are found fully conserved. Strikingly, most of the candidates do not display a classical viral-like frameshift signal and would have escaped a search based on current models of frameshifting. These results strongly suggest that −1 frameshifting might be more widely distributed than previously thought.Sequencing programs, along with various projects in the pharmaceutical, agricultural, aquacultural, and forestry industries, are creating an explosion of DNA sequence data. With this abundance of data, there is a growing need for more effective tools and methods to extract vital information from raw DNA sequences. Algorithms for identifying protein-coding regions and predicting complete genes are of particular importance. Since the early 1990s, a number of computer programs for eukaryotic gene identification have been developed: GENMARK (Borodovsky and

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Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p

Cited by 38 publications

References 42 publications

A hint for the function of human Sco1 from different structures

A hint for the function of human Sco1 from different structures

Crystal Structure of Human SCO1

Identification of programmed translational -1 frameshifting sites in the genome of Saccharomyces cerevisiae

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